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Volumn 24, Issue 2, 2015, Pages 174-181

Intrinsic flexibility of NLRP pyrin domains is a key factor in their conformational dynamics, fold stability, and dimerization

Author keywords

charge relay system; conformational dynamics; entropy; fold stability; molecular dynamics simulation; NLRP dimerization; NLRP14 signaling; pyrin domain

Indexed keywords

CRYOPYRIN; NLRP14 PROTEIN, HUMAN; NLRP4 PROTEIN, HUMAN; NUCLEOSIDE TRIPHOSPHATASE; REPRESSOR PROTEIN;

EID: 84924349031     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2601     Document Type: Article
Times cited : (23)

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